Crystal structure of the human dual specificity phosphatase 1 catalytic domain

Protein Sci. 2018 Feb;27(2):561-567. doi: 10.1002/pro.3328. Epub 2017 Nov 21.


The dual specificity phosphatase DUSP1 was the first mitogen activated protein kinase phosphatase (MKP) to be identified. It dephosphorylates conserved tyrosine and threonine residues in the activation loops of mitogen activated protein kinases ERK2, JNK1 and p38-alpha. Here, we report the crystal structure of the human DUSP1 catalytic domain at 2.49 Å resolution. Uniquely, the protein was crystallized as an MBP fusion protein in complex with a monobody that binds to MBP. Sulfate ions occupy the phosphotyrosine and putative phosphothreonine binding sites in the DUSP1 catalytic domain.

Keywords: DUSP; crystallization chaperone; dual specificity phosphatase; maltose-binding protein; monobody; sulfate ions.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, N.I.H., Intramural

MeSH terms

  • Binding Sites
  • Catalytic Domain
  • Crystallography, X-Ray
  • Dual Specificity Phosphatase 1 / chemistry*
  • Dual Specificity Phosphatase 1 / metabolism*
  • Humans
  • Maltose-Binding Proteins / metabolism*
  • Models, Molecular
  • Phosphothreonine / chemistry
  • Phosphotyrosine / chemistry
  • Protein Conformation
  • Substrate Specificity
  • Sulfates / chemistry


  • Maltose-Binding Proteins
  • Sulfates
  • Phosphothreonine
  • Phosphotyrosine
  • DUSP1 protein, human
  • Dual Specificity Phosphatase 1

Associated data

  • PDB/6APX